Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium

Stepan S. Denisov; Alexandra C. A. Heinzmann; Tanja Vajen; Mark H. M. Vries; Remco T. A. Megens; Dennis Suylen; Rory R. Koenen; Mark J. Post; Johannes H. Ippel; Tilman M. Hackeng; Ingrid Dijkgraaf

doi:10.1021/acs.bioconjchem.0c00095

Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium

Stepan S. Denisov, Alexandra C. A. Heinzmann, Tanja Vajen, Mark H. M. Vries, Remco T. A. Megens, Dennis Suylen, Rory R. Koenen, Mark J. Post, Johannes H. Ippel, Tilman M. Hackeng, Ingrid Dijkgraaf^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.

Original language	English
Pages (from-to)	948-955
Number of pages	8
Journal	Bioconjugate Chemistry
Volume	31
Issue number	3
DOIs	https://doi.org/10.1021/acs.bioconjchem.0c00095
Publication status	Published - 20 Feb 2020

Keywords

MONOCYTE RECRUITMENT
BINDING
ATHEROSCLEROSIS
NEUTROPHILS
EXPRESSION
ARREST

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10.1021/acs.bioconjchem.0c00095Licence: CC BY-NC-ND

Cite this

Denisov, S. S., Heinzmann, A. C. A., Vajen, T., Vries, M. H. M., Megens, R. T. A., Suylen, D., Koenen, R. R., Post, M. J., Ippel, J. H., Hackeng, T. M., & Dijkgraaf, I. (2020). Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium. Bioconjugate Chemistry, 31(3), 948-955. https://doi.org/10.1021/acs.bioconjchem.0c00095

@article{0621299583f142cb81d4b43ba6a7b73d,

title = "Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium",

abstract = "Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.",

keywords = "MONOCYTE RECRUITMENT, BINDING, ATHEROSCLEROSIS, NEUTROPHILS, EXPRESSION, ARREST",

author = "Denisov, {Stepan S.} and Heinzmann, {Alexandra C. A.} and Tanja Vajen and Vries, {Mark H. M.} and Megens, {Remco T. A.} and Dennis Suylen and Koenen, {Rory R.} and Post, {Mark J.} and Ippel, {Johannes H.} and Hackeng, {Tilman M.} and Ingrid Dijkgraaf",

note = "Funding Information: This study was in part performed within the framework of the Center for Translational Molecular Medicine (CTMM), project EMINENCE (grant 01C-204 to M.J.P.; T.M.H.), and in part made possible by The Netherlands Organisation for Scientific Research (NWO; VIDI 723.013.009 and Aspasia 015.010.005 to I.D.) and the Landsteiner Foundation for Blood Transfusion Research (LSBR Nr. 1638, to R.R.K.). Jacques Debets, and Jeroen Hameleers are greatly acknowledged for their assistance with the mouse carotid experiments. Publisher Copyright: {\textcopyright} 2020 American Chemical Society.",

year = "2020",

month = feb,

day = "20",

doi = "10.1021/acs.bioconjchem.0c00095",

language = "English",

volume = "31",

pages = "948--955",

journal = "Bioconjugate Chemistry",

issn = "1043-1802",

publisher = "American Chemical Society",

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Denisov, SS, Heinzmann, ACA, Vajen, T, Vries, MHM, Megens, RTA, Suylen, D, Koenen, RR , Post, MJ , Ippel, JH , Hackeng, TM & Dijkgraaf, I 2020, 'Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium', Bioconjugate Chemistry, vol. 31, no. 3, pp. 948-955. https://doi.org/10.1021/acs.bioconjchem.0c00095

Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium. / Denisov, Stepan S.; Heinzmann, Alexandra C. A.; Vajen, Tanja et al.
In: Bioconjugate Chemistry, Vol. 31, No. 3, 20.02.2020, p. 948-955.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium

AU - Denisov, Stepan S.

AU - Heinzmann, Alexandra C. A.

AU - Vajen, Tanja

AU - Vries, Mark H. M.

AU - Megens, Remco T. A.

AU - Suylen, Dennis

AU - Koenen, Rory R.

AU - Post, Mark J.

AU - Ippel, Johannes H.

AU - Hackeng, Tilman M.

AU - Dijkgraaf, Ingrid

N1 - Funding Information: This study was in part performed within the framework of the Center for Translational Molecular Medicine (CTMM), project EMINENCE (grant 01C-204 to M.J.P.; T.M.H.), and in part made possible by The Netherlands Organisation for Scientific Research (NWO; VIDI 723.013.009 and Aspasia 015.010.005 to I.D.) and the Landsteiner Foundation for Blood Transfusion Research (LSBR Nr. 1638, to R.R.K.). Jacques Debets, and Jeroen Hameleers are greatly acknowledged for their assistance with the mouse carotid experiments. Publisher Copyright: © 2020 American Chemical Society.

PY - 2020/2/20

Y1 - 2020/2/20

N2 - Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.

AB - Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.

KW - MONOCYTE RECRUITMENT

KW - BINDING

KW - ATHEROSCLEROSIS

KW - NEUTROPHILS

KW - EXPRESSION

KW - ARREST

U2 - 10.1021/acs.bioconjchem.0c00095

DO - 10.1021/acs.bioconjchem.0c00095

M3 - Article

C2 - 32077689

SN - 1043-1802

VL - 31

SP - 948

EP - 955

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

IS - 3

ER -